Artificial fibers from globular and fibrous proteins



' of proteins, which can both classes of natural Patented Dec. 31, 1946I ART1FICIAL FIBERS mom GLOBULAB AND masons rao'rams Oskar Huppert, NewYork, N. Y.

No Drawing. Application February 12,1945, Serial No. 577,593

serum. (01. 260-119) a continuation in part of theone filed on May 24,1944, bearing Serial No. 537,190, now U. S. Patent 2,384,421. Myinvention deals'with fibers made from proteins. The object ofthis'invention is to produce dispersions I be used to make fibers, whichhave strength, water resistance, flexibility and softness and arevaluable as fibers.

A further object resides in processes for making these dispersions.Other objects of the invention will appear as the description proceeds.

These objects are accomplished by the follow- This application is inginvention in which dispersions of pseudothiohydantoin-protein salts ofalkyl-benzene su'lionic acid of the general formula as follows:

CHr--S\ I wherein; protein-NHz denotes protein, are used to produceartificial fibers from globular and fibrous proteins by spinning andstretching, hardening, pre and after treatment methods with variousmodifyingagents already known to the art. All proteins d that thereaction takes place I have discov I rnmonia, where a protein is also inpresenc used which {woiil side of its fisfoelectric point. According tothis invention fibers may be prepared either from an ammoniaalkaline-aqueous solution where a protein is used as forinstance'casein, soybean or peanut protein, egg albumin, reduced.chicken feather keratin .or from an alcoholic-aqueous solution where aprotein is, used as for instance zein, gliadin or. otherfprqlamines,protamines. The present;i dea hf structural units or natural fibers asstemolecules developed by gistbury, Mark andMeyer and others are not ableto disclose the structural difie' ence of globular and fibrous proteins.My;work to establish the structure of th rot ins starts from earlystatements, publis Konstitution und Konfig- .uration der and is used inthe present application. Textile fibers should have strength andflexibility. Globular (sphero) proteins as such are not fit forpreparing fibers, only fibrillar (linear). proteins are, capable offorming fibers which in certain circumstances are sufiiciently tough ande precipitated on the acidstofie, Wien-Liepzig, 1928, so

- pattern of folds. On

contracted. More .or less cross linked by means of secondary valenc'esthrough polar groups, salt linkages they form with their side chains acoplanar three dimensional arrangement. Because of free rotation aroundsingle bonds the structural units of natural fibers arecapable of beingoriented and to form crystal lattices which favors fiber strength andflexibility, pletely cross linking.

The current view of globular protein accord-- ing X-ray analysis is thatcrystalline globular proteins have a compact structure, that the veryregularly built molecules contain a considerable amount of water. Thevery highly ordered structure, revealed by .X-ray photographs ofprotein. crystals, discloses, that the chains of the globular proteinsmust be built into a very systematic agents a breakdown of this specialordered structure occurs and the resulting products aggregate oncoagulation into fibrous bundles which have been shown in my publicationelastic to possess some technical interest. These by'X-ray study to beof the beta keratin type. An intimate relation between the fibrous andthe globular proteins is'there- Therefore a transformation of globularproteins in fibrous proteins should be possible. However, neither thecyclol hypothesis of D. M. Wrinch (1936) nor the models of Huggins(1940) have shown wherein the special configuration of the chains of theglobular proteins consists and the X-ray' diffraction patterns of theglobular proteins are still not sufiiciently advanced.

Based on the reaction of carbon disulfide -and proteins, proteinhydrolysates, alpha amino acids, U. S. Patent 2,112,210 and on andphysical-biochemical reactions of natural, native proteins in the livingorganism I conceived Das Protein Wien, 1933, the Accordingly allglobular prothe same general pattern with indicated.

Proteyl-theory. .teins are built up on from normal proteyls,

in =5 0H or from pseudo-proteyls, I

a a I which six of each are in space configurated under an angle of 60degrees in the boat type, representingthe isomeres of the elementaryunits. of the protein. The elementary unit exists in threestereoisomeric forms. The normal form showing relations withdioxopiperazines, oxazolines, triazines, acetaldehyde, hexoses,hexosamines, glucose, the purin form with beta ketonic acids, acetone,pyridine, purin and pyrimidine glucosides, purin bases such as it thereis not com-- treatment with denaturatin the physiological the pseudoform with 3 adenine, guanine and pyrimidine bases. such as cytosine anduracil, the combined normal-pseudo form with isoprene, phytol, terpenederivatives and carotenoides. The following formulas give the structureand configuration of the elementary I units of the protein:

THE ELEMENTARY ISOMERES OF Two such normal proteyls, belonging .to' twodifferent elementary units, would formally result by condensation of twomol alpha amino acids in the zwitter ion form as follows: in NHw Bshowing the peptide-betain linkage encircled.

UNITSOF -minative' factor for their the following composition:

This network of proteyls changes in a bundle of polypeptide chainsresulting from the conversion of the peptide-betain linkage in apeptidelinkageas follows:

Any non-protcolytic modification of the unique structure of a nativeprotein resulting under the influence of denaturating agents is a stepin the continuous line of a dynamic process leading from the verysystematic. and specific 'pattern of the six in space conflguratedp'roteyls under breakdown of the proteyl-girder to unfolded polypeptidechains of the beta keratin type with the intermediate stages of supercontracted and coiled polypeptide chains.

Associating water as well on the polar, hydrophilic groups of their sidechains (external hydration) as, on the oxygen atoms of the girder, thhydration degree of the proteins turns out to be decisive for theosmotic pressure and-viscosities of the protein solutions while thedenaturation-kinetic of the proteins becomes the deterability to be spunin fibers.

Solutions containing salts of pseudothiohydantoin-protein (fibrous andglobular). with alkyl-benzene sulfonic acids'can be used to .precipitatethe synthetic protein in a coagulating bath into a, plastic state,favorable for drawing into fibers. 'On the alkaline side of theisoelectric point anions of the alkyl-benzene sulfonic acid exert aninfluence conducive to the transformation or the globular proteins infibrous proteins by drawing the fibers over 300%.

The following examples are illustrative for all proteins and will serveto show certain specific details of the invention, however, it is to, beunder stood that the specific details as set forth in the examples arenot to be considered as limitative of the invention. E rample 1 asolution having 110 grams of casein are'soaked in 555 cc. of water at 24C. containing 9.4 'g. monochloracetic acid, 7.6 g. ammonium thiocyanate,8.1 g.'p-toluene sulfonic acid cryst. and 21 cc. concentrated ammoniumhydroxide with stirring. After three hours the dispersion is heated to45 C. and the ripened and deaerated solutionis forced through aspinneret of forty holes and of a diameter of 0.004 inch into acoagulating bath having the composition: water cc., conc. sulfuric acid15 g., anhydrous sodium Casein fibers are spun from sulfate 20 g.,aluminum sulfate (hydrate) 10 g.

The coagulated fibers are afterwards stretched in sodium chloride at atema bathcontaining 15% hed perature over 50 C. The fibers are now wasand dried without tension.

Example 2 Soya bean protein fibers are spun from a solution having thefollowing composition:

Water cc' 806 Monochloracetic' acid; g 15 Aminoniumthiocyanate g 12p-Toluene sulfonic acid cryst -g 13 Concentrated ammonium hydroxide cc33 Alpha soya bean' protein g 180 protein for 30 minutes at a C. thedispersion is warmed The spinnin After soaking the temperature of 45 to65 C. and mixed under stirring.

v solution after permitting to mature is then forced under stretchingthrough a spinneret into a coagulating bath as follows:

Water per cent 55 Acid sulfuric -do 25 Sodium sulfate do 20 TemperatureC 45 The fibers are afterwards thoroughly washed and dried withouttension, using a current of air, after they were hardened in a bath asfollows:

i Per cent Water 9 Formaldehyde 4 Sodium chloride 1 Example 3 Fibersfrom zein are prepared by extrusion of a solution, which isobtainedbydissolving in a mixture of 300 cc. of denatured alcohol and 36 cc. ofwater 1.8 g. monochloracetic acid, 1.35 g. ammoniu'mthiocyanate and 1.5g. p-toluene-sulfonic acid cryst. and after addition of 90 g. of zein byheating under stirring for a half hour. The spinneret used is the usualforty holes viscose spinneret and the coagulating bath consists of 5%aluminum sulfate. After washing the filaments are stretched in warmwater and then passed into cold water and treated with 6% formaldehydesolution. The fibers are washed with cold water again and dried.

Havingnow'particularly described and ascertained the nature of my saidinvention, I declare that what I claim is. 1

1; As a new article or manufacture, a fiber consisting of analkyl-benzene-sulfonic acid salt of a pseudothiohydantoin, substitutedin position 3 by a protein radical selected from the group consisting ofphospho-proteins, globulins and prolarnines, having the formula:

wherein protein represents the residue of a -protein molecule afterremoval of NHz-- therefrom.

3. As a new article of manufacture, a fiber consisting of a paratoluene-sulfonic acid salt of pseudothiohydantoin, substituted inposition 3 by the radical of casein, having the formula:

ou -s casein whereincasein' represents the residue of a casein moleculeafter removal of NH2- therefrom.

OSKAR HUPPERT.

